SIGM1_REOVL
ID SIGM1_REOVL Reviewed; 470 AA.
AC P04506; A4ZY30; P07937;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 02-JUN-2021, entry version 113.
DE RecName: Full=Outer capsid protein sigma-1;
DE Short=Sigma1;
DE AltName: Full=Cell attachment protein;
DE AltName: Full=Hemagglutinin;
GN Name=S1;
OS Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10884;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3855545; DOI=10.1073/pnas.82.1.24;
RA Cashdollar L.W., Chmelo R.A., Wiener J.R., Joklik W.K.;
RT "Sequences of the S1 genes of the three serotypes of reovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:24-28(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2430568; DOI=10.1016/0006-291x(86)90761-8;
RA Munemitsu S.M., Atwater J.A., Samuel C.E.;
RT "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning
RT and nucleotide sequence of the reovirus serotype 1 Lang strain bicistronic
RT s1 mRNA which encodes the minor capsid polypeptide sigma 1a and the
RT nonstructural polypeptide sigma 1bNS.";
RL Biochem. Biophys. Res. Commun. 140:508-514(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2305549; DOI=10.1016/0042-6822(90)90093-7;
RA Duncan R., Horne D., Cashdollar L.W., Joklik W.K., Lee P.W.K.;
RT "Identification of conserved domains in the cell attachment proteins of the
RT three serotypes of reovirus.";
RL Virology 174:399-409(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2335823; DOI=10.1128/jvi.64.6.2976-2989.1990;
RA Nibert M.L., Dermody T.S., Fields B.N.;
RT "Structure of the reovirus cell-attachment protein: a model for the domain
RT organization of sigma 1.";
RL J. Virol. 64:2976-2989(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone;
RX PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA Wilson G.J., Chappell J.D., Dermody T.S.;
RT "A plasmid-based reverse genetics system for animal double-stranded RNA
RT viruses.";
RL Cell Host Microbe 1:147-157(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21.
RX PubMed=6158163; DOI=10.1016/0042-6822(80)90154-3;
RA Li J.K.-K., Keene J.D., Scheible P.P., Joklik W.K.;
RT "Nature of the 3'-terminal sequences of the plus and minus strands of the
RT S1 gene of reovirus serotypes 1, 2 and 3.";
RL Virology 105:41-51(1980).
CC -!- FUNCTION: Fiber-like molecule that attaches the virion to the host cell
CC membrane by binding to the primary receptor F11R/JAM-A and to sialic
CC acid containing proteins (coreceptor). The interaction of sigma-1 with
CC F11R is required for NF-kB activation and apoptosis. Binding to both
CC sialic acid and F11R is required to induce maximal levels of apoptosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts (via the head region) with human F11R
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Found in the outer
CC capsid (36 copies). {ECO:0000250}.
CC -!- PTM: Undergoes dramatic conformational rearrangements during viral
CC disassembly in the endocytic pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47276.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA66877.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M10260; AAA66877.1; ALT_FRAME; Genomic_RNA.
DR EMBL; M14779; AAA47276.1; ALT_FRAME; Genomic_RNA.
DR EMBL; M32860; AAA47267.1; -; Genomic_RNA.
DR EMBL; M35963; AAA47242.1; -; Genomic_RNA.
DR EMBL; EF494445; ABP48923.1; -; Genomic_RNA.
DR EMBL; AH002406; AAA47240.1; -; Genomic_RNA.
DR PIR; A04122; HMXRH1.
DR PIR; A34829; HMXRL1.
DR PDB; 4GU3; X-ray; 3.60 A; A/B/C=261-470.
DR PDB; 4GU4; X-ray; 3.50 A; A/B/C=261-470.
DR PDB; 4ODB; X-ray; 3.20 A; A/B/C=308-470.
DR PDB; 4XC5; X-ray; 2.20 A; A/B/C=308-470.
DR PDB; 5MHS; X-ray; 3.70 A; A/B/C=308-470.
DR PDB; 6GAJ; X-ray; 1.35 A; A/B/C=29-159.
DR PDB; 6GAK; X-ray; 1.43 A; A/B/C=29-159.
DR PDB; 6GAO; X-ray; 2.10 A; A/B/C=29-264.
DR PDBsum; 4GU3; -.
DR PDBsum; 4GU4; -.
DR PDBsum; 4ODB; -.
DR PDBsum; 4XC5; -.
DR PDBsum; 5MHS; -.
DR PDBsum; 6GAJ; -.
DR PDBsum; 6GAK; -.
DR PDBsum; 6GAO; -.
DR SMR; P04506; -.
DR ABCD; P04506; 1 sequenced antibody.
DR Proteomes; UP000007253; Genome.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR008982; Adenovirus_pIV-like_att.
DR InterPro; IPR002592; Vir_attach_sigma1_reovir.
DR Pfam; PF01664; Reo_sigma1; 1.
DR SUPFAM; SSF49835; SSF49835; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Glycoprotein; Hemagglutinin;
KW Host-virus interaction; Outer capsid protein; Reference proteome;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..470
FT /note="Outer capsid protein sigma-1"
FT /id="PRO_0000040667"
FT REGION 1..324
FT /note="Tail"
FT REGION 325..470
FT /note="Head"
FT COILED 26..46
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 91
FT /note="V -> G (in Ref. 1; AAA66877 and 2; AAA47276)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> F (in Ref. 1; AAA66877)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="V -> L (in Ref. 2; AAA47276)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="L -> W (in Ref. 4; AAA47242)"
FT /evidence="ECO:0000305"
FT HELIX 30..156
FT /evidence="ECO:0007829|PDB:6GAJ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6GAO"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6GAO"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6GAO"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4GU4"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4GU4"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4GU4"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:4GU4"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4GU4"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4XC5"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4XC5"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 333..345
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 348..361
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:4XC5"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:4ODB"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 423..437
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 440..449
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:4XC5"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:4XC5"
SQ SEQUENCE 470 AA; 51404 MW; F4D18989AD54491C CRC64;
MDASLITEIR KIVLQLSVSS NGSQSKEIEE IKKQVQVNVD DIRAANIKLD GLGRQIADIS
NSISTIESRL GEMDNRLVGI SSQVTQLSNS VSQNTQSISS LGDRINAVEP RVDSLDTVTS
NLTGRTSTLE ADVGSLRTEL AALTTRVTTE VTRLDGLINS GQNSIGELST RLSNVETSMV
TTAGRGLQKN GNTLNVIVGN GMWFNSSNQL QLDLSGQSKG VGFVGTGMVV KIDTNYFAYN
SNGEITLVSQ INELPSRVST LESAKIDSVL PPLTVREASG VRTLSFGYDT SDFTIINSVL
SLRSRLTLPT YRYPLELDTA NNRVQVADRF GMRTGTWTGQ LQYQHPQLSW RANVTLNLMK
VDDWLVLSFS QMTTNSIMAD GKFVINFVSG LSSGWQTGDT EPSSTIDPLS TTFAAVQFLN
NGQRIDAFRI MGVSEWTDGE LEIKNYGGTY TGHTQVYWAP WTIMYPCNVR